Tau impacts on growth-factor-stimulated actin remodeling.

Abstract:

:The microtubule-associated protein tau interacts with the SH3 domain of non-receptor Src family protein tyrosine kinases. A potential consequence of the SH3 interaction is the upregulation of tyrosine kinase activity. Here we investigated the activation of Src or Fyn by tau, both in vitro and in vivo. Tau increased the kinase activity in in vitro assays and in transfected COS7 cells. In platelet-derived growth factor (PDGF)-stimulated fibroblasts, tau appeared to prime Src for activation following PDGF stimulation, as reflected by changes in Src-mediated actin rearrangements. In addition, while fibroblasts normally recovered actin stress fibers by 5-7 hours after PDGF stimulation, tau-expressing cells showed sustained actin breakdown. Microtubule association by tau was not required for the observed changes in actin morphology. Inhibition of Src kinases or a mutant deficient in Src interaction reduced the effects, implicating Src family protein tyrosine kinases as a mediator of the effects of tau on actin rearrangements. Our results provide evidence that the interaction of tau with Src upregulates tyrosine kinase activity and that this interaction allows tau to impact on growth-factor-induced actin remodeling.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Sharma VM,Litersky JM,Bhaskar K,Lee G

doi

10.1242/jcs.03378

subject

Has Abstract

pub_date

2007-03-01 00:00:00

pages

748-57

issue

Pt 5

eissn

0021-9533

issn

1477-9137

pii

jcs.03378

journal_volume

120

pub_type

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